ArticleBiochemistry2012
The native GCN4 leucine-zipper domain does not uniquely specify a dimeric oligomerization state.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Manipulating the Unfolded State of a Folded Protein through Site-Specific Backbone Modification.Biochemistry · 2026Article
- Chloride Binding in Trimeric Coiled Coils: Free Energy and Structural Determinants from Molecular Simulations.Journal of chemical information and modeling · 2026Article
- Sequence Prediction, Structural Modelling and the Challenges of Plasticity in Coiled Coils.Sub-cellular biochemistry · 2026Review
- Grafted Coiled-Coil Peptides as Multivalent Scaffolds for Protein Recognition.ACS chemical biology · 2025Article
- A Designed ZnJournal of the American Chemical Society · 2025Article
- Proteomimetic Strategy for the Modulation of Intrinsically Disordered Protein MYC.Journal of the American Chemical Society · 2025Article
- Multimerization of a disordered kinetochore protein promotes accurate chromosome segregation by localizing a core dynein module.The Journal of cell biology · 2024Article
- Fast clearance of platelets in a commonly used mouse model for GPIbα is impeded by an anti-GPIbβ antibody derivative.Journal of thrombosis and haemostasis : JTH · 2022Article
- An Unusual Aspartic Acid Cluster in the Reovirus Attachment Fiber σ1 Mediates Stability at Low pH and Preserves Trimeric Organization.Journal of virology · 2022Article
- Prerequisites for Stabilizing Long-Range Synergistic Interactions amongBiochemistry · 2022Article
- A nanobody toolbox targeting dimeric coiled-coil modules for functionalization of designed protein origami structures.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structural insights into the tropomodulin assembly at the pointed ends of actin filaments.Protein science : a publication of the Protein Society · 2021Article
- Designs and Characterization of Subunit Ebola GP Vaccine Candidates: Implications for Immunogenicity.Frontiers in immunology · 2020Article
- Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO.Journal of visualized experiments : JoVE · 2019Article
- The IKK-binding domain of NEMO is an irregular coiled coil with a dynamic binding interface.Scientific reports · 2019Article
- Article
- Atomistic simulations indicate the functional loop-to-coiled-coil transition in influenza hemagglutinin is not downhill.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Conformational Dynamics of Asparagine at Coiled-Coil Interfaces.Biochemistry · 2017Article
- Design of coiled-coil protein-origami cages that self-assemble in vitro and in vivo.Nature biotechnology · 2017Article
- How order and disorder within paramyxoviral nucleoproteins and phosphoproteins orchestrate the molecular interplay of transcription and replication.Cellular and molecular life sciences : CMLS · 2017Review
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5 authors.
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Abstract
The dimerization domain of the yeast transcription factor GCN4, one of the first coiled-coil proteins to be structurally characterized at high resolution, has served as the basis for numerous fundamental studies on α-helical folding. Mutations in the GCN4 leucine zipper are known to change its preferred oligomerization state from dimeric to trimeric or tetrameric; however, the wild-type sequence has been assumed to encode a two-chain assembly exclusively. Here we demonstrate that the GCN4 coiled-coil domain can populate either a dimer or trimer fold, depending on environment. We report high-resolution crystal structures of the wild-type sequence in dimeric and trimeric assemblies. Biophysical measurements suggest populations of both oligomerization states under certain experimental conditions in solution. We use parallel tempering molecular dynamics simulations on the microsecond time scale to compare the stability of the dimer and trimer folded states in isolation. In total, our results suggest that the folding behavior of the well-studied GCN4 leucine-zipper domain is more complex than was previously appreciated. Our results have implications in ongoing efforts to establish predictive algorithms for coiled-coil folds and the selection of coiled-coil model systems for design and mutational studies where oligomerization state specificity is an important consideration.
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